Secretion of psychrophilic α-amylase deletion mutants in Pseudoalteromonas haloplanktis TAC125

Abstract

The nature and location of structural features responsible for the secretion of a cold-adapted α-amylase in the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125 was studied by deletion mutagenesis of the wild-type enzyme and of chimerical proteins derived from the fusion of the α-amylase with a reporter enzyme. Domain C of the psychrophilic α-amylase contains secretion features involved in extracellular targeting. © 2006 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved.